Ryanodine receptors: structure, expression, molecular details, and function in calcium release.

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Lanner JT, Georgiou DK, Joshi AD, Hamilton SL

Ryanodine receptors: structure, expression, molecular details, and function in calcium release.

Cold Spring Harb Perspect Biol. 2010 Nov;2(11):a003996. doi: 10.1101/cshperspect.a003996. Epub 2010 Oct 20.

PubMed ID

20961976 [ View in PubMed

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Abstract

Ryanodine receptors (RyRs) are located in the sarcoplasmic/endoplasmic reticulum membrane and are responsible for the release of Ca(2+) from intracellular stores during excitation-contraction coupling in both cardiac and skeletal muscle. RyRs are the largest known ion channels (> 2MDa) and exist as three mammalian isoforms (RyR 1-3), all of which are homotetrameric proteins that interact with and are regulated by phosphorylation, redox modifications, and a variety of small proteins and ions. Most RyR channel modulators interact with the large cytoplasmic domain whereas the carboxy-terminal portion of the protein forms the ion-conducting pore. Mutations in RyR2 are associated with human disorders such as catecholaminergic polymorphic ventricular tachycardia whereas mutations in RyR1 underlie diseases such as central core disease and malignant hyperthermia. This chapter examines the current concepts of the structure, function and regulation of RyRs and assesses the current state of understanding of their roles in associated disorders.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Tetracaine	Ryanodine receptor 1	Protein	Humans	Yes	Modulator	Details
Tetracaine	Ryanodine receptor 2	Protein	Humans	Yes	Modulator	Details

Polypeptides

Name	UniProt ID
Ryanodine receptor 1	P21817	Details
Ryanodine receptor 2	Q92736	Details